ID U3FWW4_MICFL Unreviewed; 211 AA.
AC U3FWW4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU368105};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU368105};
DE AltName: Full=GST class-pi {ECO:0000256|RuleBase:RU368105};
OS Micrurus fulvius (Eastern coral snake) (Coluber fulvius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=8637 {ECO:0000313|EMBL:JAB54136.1};
RN [1] {ECO:0000313|EMBL:JAB54136.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAB54136.1};
RX PubMed=23915248; DOI=10.1186/1471-2164-14-531;
RA Margres M.J., Aronow K., Loyacano J., Rokyta D.R.;
RT "The venom-gland transcriptome of the eastern coral snake (Micrurus
RT fulvius) reveals high venom complexity in the intragenomic evolution of
RT venoms.";
RL BMC Genomics 14:531-531(2013).
RN [2] {ECO:0000313|EMBL:JAI09951.1}
RP NUCLEOTIDE SEQUENCE.
RA Margres M.J., Wray K.P., McGivern J.J., Seavy M., Sanader D., Facente J.,
RA Rokyta D.R.;
RT "The extremes of toxin expression variation revealed in two sympatric snake
RT species.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU368105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|RuleBase:RU368105};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368105}.
CC Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus
CC {ECO:0000256|RuleBase:RU368105}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC {ECO:0000256|ARBA:ARBA00007297, ECO:0000256|RuleBase:RU368105}.
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DR EMBL; GAEP01000685; JAB54136.1; -; mRNA.
DR EMBL; GBEW01000414; JAI09951.1; -; mRNA.
DR AlphaFoldDB; U3FWW4; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03210; GST_C_Pi; 1.
DR CDD; cd03076; GST_N_Pi; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU368105};
KW Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW Nucleus {ECO:0000256|RuleBase:RU368105};
KW Transferase {ECO:0000256|RuleBase:RU368105, ECO:0000313|EMBL:JAB54136.1}.
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 84..204
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 211 AA; 23808 MW; DF32EDE9D1136318 CRC64;
MPGEYTLTYF PVRGRGEAIR MLMADQGQEW TEDVVNGEIW KKGDLKKLCA FGQLPRFQDG
NFILHQSNAI LRHLARNHGL YGEDAKEAAL LDMVNDGVED LRIKYARLIY QNYESGKAAY
IEALPAELDP FEKLLAQNDG GKGFIVGKQI GFADYNLLDI LHVHLVLASN CLASLPLLAG
YVQRLNDRPR LKNFLESDAR KKRFINGNGK Q
//
